Linked Life Data

9781874

Source:http://linkedlifedata.com/resource/pubmed/id/9781874

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-12-8
pubmed:abstractText
The Schizosaccharomyces pombe cwg2+ gene encodes the beta-subunit of geranylgeranyl transferase I (GGTase I), which participates in the post-translational C-terminal modification of several small GTPases, allowing their targeting to the membrane. Using the two-hybrid system, we have identified the cwp1+ gene that encodes the alpha-subunit of the GGTase I. cwp1p interaction with cwg2p was mapped to amino acids 1-244 or 137-294 but was not restricted to amino acids 137-244. The genomic cwp1+ was isolated and sequenced. It has two putative open reading frames of 677 and 218 bp, separated by a 51 bp intron. The predicted amino acid sequence shows significant similarity to GGTase I alpha-subunits from different species. However, complementation of Saccharomyces cerevisiae ram2-1 mutant by overexpressing the cwp1+ gene was not possible. Expression of both cwg2+ and cwp1+ in Escherichia coli allowed 'in vitro' reconstitution of the GGTase I activity. S. pombe cells expressing the mutant enzyme containing the cwg2-1 mutation do not grow at 37 degrees C, but the growth defect can be suppressed by the addition of sorbitol. Actin immunostaining of the cwg2-1 mutant strain grown at 37 degrees C showed an abnormal distribution of actin patches. The cwg2-1 mutation was identified as a guanine to adenine substitution at nucleotide 604 of the coding region, originating the change A202T in the cwg2p. Deletion of the cwg2 gene is lethal; delta cwg2 spores can divide two or three times before losing viability. Most cells have aberrant morphology and septation defects. Overexpression of the rho1G15VC199R double-mutant allele in S. pombe caused loss of polarity but was not lethal and did not render the (1-3)beta-D-glucan synthase activity independent of GTP. Therefore, geranylgeranylation of rho1p is required for the appropriate function of this GTPase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1357-67
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:9781874-Actins, pubmed-meshheading:9781874-Alkyl and Aryl Transferases, pubmed-meshheading:9781874-Amino Acid Sequence, pubmed-meshheading:9781874-Animals, pubmed-meshheading:9781874-Base Sequence, pubmed-meshheading:9781874-DNA, Fungal, pubmed-meshheading:9781874-Escherichia coli, pubmed-meshheading:9781874-GTP-Binding Proteins, pubmed-meshheading:9781874-Gene Expression, pubmed-meshheading:9781874-Genes, Fungal, pubmed-meshheading:9781874-Humans, pubmed-meshheading:9781874-Molecular Sequence Data, pubmed-meshheading:9781874-Point Mutation, pubmed-meshheading:9781874-Protein Prenylation, pubmed-meshheading:9781874-Recombinant Fusion Proteins, pubmed-meshheading:9781874-Schizosaccharomyces, pubmed-meshheading:9781874-Schizosaccharomyces pombe Proteins, pubmed-meshheading:9781874-Sequence Homology, Amino Acid, pubmed-meshheading:9781874-Substrate Specificity, pubmed-meshheading:9781874-rho GTP-Binding Proteins
pubmed:year
1998
pubmed:articleTitle
Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe.
pubmed:affiliation
Instituto de Microbiologia Bioquimica, CSIC/Universidad de Salamanca, Edificio Departamental, Spain.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't